Please use this identifier to cite or link to this item:
doi:10.22028/D291-30941
Title: | 14-3-3 Proteins and Other Candidates form Protein-Protein Interactions with the Cytosolic C-terminal End of SOS1 Affecting Its Transport Activity |
Author(s): | Duscha, Kerstin Martins Rodrigues, Cristina Müller, Maria Wartenberg, Ruth Fliegel, Larry Deitmer, Joachim W. Jung, Martin Zimmermann, Richard Neuhaus, H. Ekkehard |
Language: | English |
Title: | International Journal of Molecular Sciences |
Volume: | 21 |
Issue: | 9 |
Publisher/Platform: | MDPI |
Year of Publication: | 2020 |
Free key words: | Arabidopsis salt tolerance salt-overly sensitive (SOS1) 14-3-3 proteins membrane transporter |
DDC notations: | 610 Medicine and health |
Publikation type: | Journal Article |
Abstract: | The plasma membrane transporter SOS1 (SALT-OVERLY SENSITIVE1) is vital for plant survival under salt stress. SOS1 activity is tightly regulated, but little is known about the underlying mechanism. SOS1 contains a cytosolic, autoinhibitory C-terminal tail (abbreviated as SOS1 C-term), which is targeted by the protein kinase SOS2 to trigger its transport activity. Here, to identify additional binding proteins that regulate SOS1 activity, we synthesized the SOS1 C-term domain and used it as bait to probe Arabidopsis thaliana cell extracts. Several 14-3-3 proteins, which function in plant salt tolerance, specifically bound to and interacted with the SOS1 C-term. Compared to wild-type plants, when exposed to salt stress, Arabidopsis plants overexpressing SOS1 C-term showed improved salt tolerance, significantly reduced Na+ accumulation in leaves, reduced induction of the salt-responsive gene WRKY25, decreased soluble sugar, starch, and proline levels, less impaired inflorescence formation and increased biomass. It appears that overexpressing SOS1 C-term leads to the sequestration of inhibitory 14-3-3 proteins, allowing SOS1 to be more readily activated and leading to increased salt tolerance. We propose that the SOS1 C-term binds to previously unknown proteins such as 14-3-3 isoforms, thereby regulating salt tolerance. This finding uncovers another regulatory layer of the plant salt tolerance program. |
DOI of the first publication: | 10.3390/ijms21093334 |
Link to this record: | urn:nbn:de:bsz:291--ds-309416 hdl:20.500.11880/30253 http://dx.doi.org/10.22028/D291-30941 |
ISSN: | 1422-0067 |
Date of registration: | 18-Dec-2020 |
Description of the related object: | Supplementary Materials |
Related object: | http://www.mdpi.com/1422-0067/21/9/3334/s1 |
Faculty: | M - Medizinische Fakultät |
Department: | M - Medizinische Biochemie und Molekularbiologie |
Professorship: | M - Keiner Professur zugeordnet |
Collections: | SciDok - Der Wissenschaftsserver der Universität des Saarlandes |
Files for this record:
File | Description | Size | Format | |
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ijms-21-03334.pdf | 2,61 MB | Adobe PDF | View/Open |
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